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Database: UniProt
Entry: A0A124JZ67_9SPHN
LinkDB: A0A124JZ67_9SPHN
Original site: A0A124JZ67_9SPHN 
ID   A0A124JZ67_9SPHN        Unreviewed;       799 AA.
AC   A0A124JZ67;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Probable phosphoketolase {ECO:0000256|HAMAP-Rule:MF_01403};
DE            EC=4.1.2.- {ECO:0000256|HAMAP-Rule:MF_01403};
GN   ORFNames=AQZ49_05705 {ECO:0000313|EMBL:KUR79473.1};
OS   Novosphingobium sp. FSW06-99.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1739113 {ECO:0000313|EMBL:KUR79473.1, ECO:0000313|Proteomes:UP000061032};
RN   [1] {ECO:0000313|EMBL:KUR79473.1, ECO:0000313|Proteomes:UP000061032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSW06-99 {ECO:0000313|EMBL:KUR79473.1,
RC   ECO:0000313|Proteomes:UP000061032};
RA   Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J.,
RA   Glaeser S.;
RT   "Draft genome sequence of Novosphingobium sp. FSW06-99 (=LMG 27919), a
RT   Novosphingobium acidiphilum related species isolated from a surface water
RT   sample of the southwest basin of Lake Grosse Fuchskuhle.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964,
CC         ECO:0000256|HAMAP-Rule:MF_01403};
CC   -!- SIMILARITY: Belongs to the XFP family. {ECO:0000256|ARBA:ARBA00005623,
CC       ECO:0000256|HAMAP-Rule:MF_01403}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUR79473.1}.
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DR   EMBL; LLZQ01000005; KUR79473.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A124JZ67; -.
DR   STRING; 1739113.AQZ49_05705; -.
DR   Proteomes; UP000061032; Unassembled WGS sequence.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd02011; TPP_PK; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   HAMAP; MF_01403; Phosphoketolase; 1.
DR   InterPro; IPR023962; Phosphoketolase.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005593; Xul5P/Fru6P_PKetolase.
DR   InterPro; IPR018969; Xul5P/Fru6P_PKetolase_C.
DR   InterPro; IPR019790; Xul5P/Fru6P_PKetolase_CS.
DR   InterPro; IPR018970; Xul5P/Fru6P_PKetolase_N.
DR   InterPro; IPR019789; Xul5P/Fru6P_PKetolase_ThDP_BS.
DR   PANTHER; PTHR31273; PHOSPHOKETOLASE-RELATED; 1.
DR   PANTHER; PTHR31273:SF0; PHOSPHOKETOLASE-RELATED; 1.
DR   Pfam; PF03894; XFP; 1.
DR   Pfam; PF09363; XFP_C; 1.
DR   Pfam; PF09364; XFP_N; 1.
DR   PIRSF; PIRSF017245; Phosphoketolase; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   PROSITE; PS60002; PHOSPHOKETOLASE_1; 1.
DR   PROSITE; PS60003; PHOSPHOKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01403};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061032};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW   Rule:MF_01403}.
FT   DOMAIN          14..377
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09364"
FT   DOMAIN          595..797
FT                   /note="Xylulose 5-phosphate/Fructose 6-phosphate
FT                   phosphoketolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09363"
SQ   SEQUENCE   799 AA;  87667 MW;  310878F644584CBD CRC64;
     MALRSTGLAT LDPVEAALID AWWRAANYLS VGQIYLYDNP LLRDPLTLDH VKPLVVGHWG
     TTPGQTFIYA HLNRVIVSHD LDMIYIAGPG HGGPALVGAT YLEGSYSEVY PGISRDTAGL
     KKLFTQFSFP GGISSHVAPT TPGSIHEGGE LGYSLSHAFG AAFDNPDLIV ACVIGDGEAE
     TGPLATAWHS NKFLSARTDG AVLPILHLNG YKISNPTVLA RIDPADLENL LTGYGWAPLF
     VEGDDPAVMH QTMARAMDTA IAAIRRIQDD ARKNPARWDE PSPMPRWPMI VLRSPKGWTG
     PKAVDGVAIE GTFHAHQVPL QVDADRPGHV ALLEAWMRSY RPEALFDDLG RLLPEIAALA
     PQGGRRMGAN PHANGGLLLR DLHLPDVHDH ACTVPAPGAI TASDMGILGT FLRDVVELNR
     ASANFRLFGP DETVSNMLDA VFDVTNRQWE EAIITHDEFL APDGRVLDAM LSEHNCEGWL
     EGYLLTGRHG IFASYEAFVR IIDSMASQHA KWLKVTAQLP WRKPIASLNL LLSSHVWQQD
     HNGFTHQDPG FLDHILTKKP AIVRAFLPPD ANCLLAVIDH CLHSRHHINV VVAGKHAMPQ
     WLTIDAAIAH CAQGIGIWKW ASNDGDADAD PDLVMAACGD TPTLEVLAAV TILRTHLPDL
     RVRVINVVDL TTLHLANEHP HGLTDADYDA LFTRTRPVIF AFHGYPGLVQ RLTHARTNRT
     LSVHGYQEEG TITTAFDIRV QNGIDRFHLV LDAIGHLPDL GSRGAWLAQT MRDKLAAHTR
     YIDVHGRDMP EIRDWVWPQ
//
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